text:
Secondary literature sources for DKCLD
The following references were automatically generated.
- Melnikov S, Ben-Shem A, Yusupova G, Yusupov M
- Insights into the origin of the nuclear localization signals in conserved ribosomal proteins.
- Nat Commun. 2015; 6: 7382-7382
- Display abstract
Eukaryotic ribosomal proteins, unlike their bacterial homologues, possess nuclear localization signals (NLSs) to enter the cell nucleus during ribosome assembly. Here we provide a comprehensive comparison of bacterial and eukaryotic ribosomes to show that NLSs appear in conserved ribosomal proteins via remodelling of their RNA-binding domains. This finding enabled us to identify previously unknown NLSs in ribosomal proteins from humans, and suggests that, apart from promoting protein transport, NLSs may facilitate folding of ribosomal RNA.
- Cerrudo CS, Mengual Gomez DL, Gomez DE, Ghiringhelli PD
- Novel insights into the evolution and structural characterization of dyskerin using comprehensive bioinformatics analysis.
- J Proteome Res. 2015; 14: 874-87
- Display abstract
Dyskerin is a conserved nucleolar protein. Several related genetic diseases are caused by defects in dyskerin. We hypothesized that having a comprehensive bioinformatic analysis of dyskerin will help to develop new drugs for this diseases. We predicted protein domains and compared sequences and structures to detect the universe of dyskerin-like proteins. We identified conserved features of shared domains in the three superkingdoms. We analyzed the phylogenetic diversity, confirming that there is a strong structural conservation. Also, we studied the relationship of dyskerin-like proteins with other proteins through an integrative protein-protein interaction approach. Most of them are conserved among homologous eukaryotic and archaeal proteins. Our results highlighted the preservation of proteins interacting with dyskerin. We identified conserved dyskerin interactor proteins between the different eukaryotes organisms. Furthermore, we studied the existence of dyskerin-like proteins in different species. Also, we compared and analyzed the secondary structure with the hydrophobic profile, confirming that all have hydrophilic properties highly conserved among proteins. The greatest difference was observed in the NTE and CTE regions. Another aspect studied was the comparison and analysis of tertiary structures. In our knowledge, this is the first time that these analyses were performed in such a comprehensive manner.
- Oulhen N, Onorato TM, Ramos I, Wessel GM
- Dysferlin is essential for endocytosis in the sea star oocyte.
- Dev Biol. 2014; 388: 94-102
- Display abstract
Dysferlin is a calcium-binding transmembrane protein involved in membrane fusion and membrane repair. In humans, mutations in the dysferlin gene are associated with muscular dystrophy. In this study, we isolated plasma membrane-enriched fractions from full-grown immature oocytes of the sea star, and identified dysferlin by mass spectrometry analysis. The full-length dysferlin sequence is highly conserved between human and the sea star. We learned that in the sea star Patiria miniata, dysferlin RNA and protein are expressed from oogenesis to gastrulation. Interestingly, the protein is highly enriched in the plasma membrane of oocytes. Injection of a morpholino against dysferlin leads to a decrease of endocytosis in oocytes, and to a developmental arrest during gastrulation. These results suggest that dysferlin is critical for normal endocytosis during oogenesis and for embryogenesis in the sea star and that this animal may be a useful model for studying the relationship of dysferlin structure as it relates to its function.
- Hurley JM, Larrondo LF, Loros JJ, Dunlap JC
- Conserved RNA helicase FRH acts nonenzymatically to support the intrinsically disordered neurospora clock protein FRQ.
- Mol Cell. 2013; 52: 832-43
- Display abstract
Protein conformation dictates a great deal of protein function. A class of naturally unstructured proteins, termed intrinsically disordered proteins (IDPs), demonstrates that flexibility in structure can be as important mechanistically as rigid structure. At the core of the circadian transcription/translation feedback loop in Neurospora crassa is the protein FREQUENCY (FRQ), shown here shown to share many characteristics of IDPs. FRQ in turn binds to FREQUENCY-Interacting RNA Helicase (FRH), whose clock function has been assumed to relate to its predicted helicase function. However, mutational analyses reveal that the helicase function of FRH is not essential for the clock, and a region of FRH distinct from the helicase region is essential for stabilizing FRQ against rapid degradation via a pathway distinct from its typical ubiquitin-mediated turnover. These data lead to the hypothesis that FRQ is an IDP and that FRH acts nonenzymatically, stabilizing FRQ to enable proper clock circuitry/function.
- Alvarez-Ponce D, Lopez P, Bapteste E, McInerney JO
- Gene similarity networks provide tools for understanding eukaryote origins and evolution.
- Proc Natl Acad Sci U S A. 2013; 110: 1594603-1594603
- Display abstract
The complexity and depth of the relationships between the three domains of life challenge the reliability of phylogenetic methods, encouraging the use of alternative analytical tools. We reconstructed a gene similarity network comprising the proteomes of 14 eukaryotes, 104 prokaryotes, 2,389 viruses and 1,044 plasmids. This network contains multiple signatures of the chimerical origin of Eukaryotes as a fusion of an archaebacterium and a eubacterium that could not have been observed using phylogenetic trees. A number of connected components (gene sets with stronger similarities than expected by chance) contain pairs of eukaryotic sequences exhibiting no direct detectable similarity. Instead, many eukaryotic sequences were indirectly connected through a "eukaryote-archaebacterium-eubacterium-eukaryote" similarity path. Furthermore, eukaryotic genes highly connected to prokaryotic genes from one domain tend not to be connected to genes from the other prokaryotic domain. Genes of archaebacterial and eubacterial ancestry tend to perform different functions and to act at different subcellular compartments, but in such an intertwined way that suggests an early rather than late integration of both gene repertoires. The archaebacterial repertoire has a similar size in all eukaryotic genomes whereas the number of eubacterium-derived genes is much more variable, suggesting a higher plasticity of this gene repertoire. Consequently, highly reduced eukaryotic genomes contain more genes of archaebacterial than eubacterial affinity. Connected components with prokaryotic and eukaryotic genes tend to include viral and plasmid genes, compatible with a role of gene mobility in the origin of Eukaryotes. Our analyses highlight the power of network approaches to study deep evolutionary events.
- Gargantini PR, Serradell MC, Torri A, Lujan HD
- Putative SF2 helicases of the early-branching eukaryote Giardia lamblia are involved in antigenic variation and parasite differentiation into cysts.
- BMC Microbiol. 2012; 12: 284-284
- Display abstract
BACKGROUND: Regulation of surface antigenic variation in Giardia lamblia is controlled post-transcriptionally by an RNA-interference (RNAi) pathway that includes a Dicer-like bidentate RNase III (gDicer). This enzyme, however, lacks the RNA helicase domain present in Dicer enzymes from higher eukaryotes. The participation of several RNA helicases in practically all organisms in which RNAi was studied suggests that RNA helicases are potentially involved in antigenic variation, as well as during Giardia differentiation into cysts. RESULTS: An extensive in silico analysis of the Giardia genome identified 32 putative Super Family 2 RNA helicases that contain almost all the conserved RNA helicase motifs. Phylogenetic studies and sequence analysis separated them into 22 DEAD-box, 6 DEAH-box and 4 Ski2p-box RNA helicases, some of which are homologs of well-characterized helicases from higher organisms. No Giardia putative helicase was found to have significant homology to the RNA helicase domain of Dicer enzymes. Additionally a series of up- and down-regulated putative RNA helicases were found during encystation and antigenic variation by qPCR experiments. Finally, we were able to recognize 14 additional putative helicases from three different families (RecQ family, Swi2/Snf2 and Rad3 family) that could be considered DNA helicases. CONCLUSIONS: This is the first comprehensive analysis of the Super Family 2 helicases from the human intestinal parasite G. lamblia. The relative and variable expression of particular RNA helicases during both antigenic variation and encystation agrees with the proposed participation of these enzymes during both adaptive processes. The putatives RNA and DNA helicases identified in this early-branching eukaryote provide initial information regarding the biological role of these enzymes in cell adaptation and differentiation.
- Jarboui MA, Wynne K, Elia G, Hall WW, Gautier VW
- Proteomic profiling of the human T-cell nucleolus.
- Mol Immunol. 2011; 49: 441-52
- Display abstract
The nucleolus, site of ribosome biogenesis, is a dynamic subnuclear organelle involved in diverse cellular functions. The size, number and organisation of nucleoli are cell-specific and while it remains to be established, the nucleolar protein composition would be expected to reflect lineage-specific transcriptional regulation of rDNA genes and have cell-type functional components. Here, we describe the first characterisation of the human T-cell nucleolar proteome. Using the Jurkat T-cell line and a reproducible organellar proteomic approach, we identified 872 nucleolar proteins. In addition to ribosome biogenesis and RNA processing networks, network modeling and topological analysis of nucleolar proteome revealed distinct macromolecular complexes known to orchestrate chromatin structure and to contribute to the regulation of gene expression, replication, recombination and repair, and chromosome segregation. Furthermore, among our dataset, we identified proteins known to functionally participate in T-cell biology, including RUNX1, ILF3, ILF2, STAT3, LSH, TCF-1, SATB1, CTCF, HMGB3, BCLAF1, FX4L1, ZAP70, TIAM1, RAC2, THEMIS, LCP1, RPL22, TOPK, RETN, IFI-16, MCT-1, ISG15, and 14-3-3tau, which support cell-specific composition of the Jurkat nucleolus. Subsequently, the nucleolar localisation of RUNX1, ILF3, STAT3, ZAP70 and RAC2 was further validated by Western Blot analysis and immunofluorescence microscopy. Overall, our T-cell nucleolar proteome dataset not only further expands the existing repertoire of the human nucleolar proteome but support a cell type-specific composition of the nucleolus in T cell and highlights the potential roles of the nucleoli in lymphocyte biology.
- Dlakic M, Mushegian A
- Prp8, the pivotal protein of the spliceosomal catalytic center, evolved from a retroelement-encoded reverse transcriptase.
- Display abstract
Prp8 is the largest and most highly conserved protein of the spliceosome, encoded by all sequenced eukaryotic genomes but missing from prokaryotes and viruses. Despite all evidence that Prp8 is an integral part of the spliceosomal catalytic center, much remains to be learned about its molecular functions and evolutionary origin. By analyzing sequence and structure similarities between Prp8 and other protein domains, we show that its N-terminal region contains a putative bromodomain. The central conserved domain of Prp8 is related to the catalytic domain of reverse transcriptases (RTs) and is most similar to homologous enzymes encoded by prokaryotic retroelements. However, putative catalytic residues in this RT domain are only partially conserved and may not be sufficient for the nucleotidyltransferase activity. The RT domain is followed by an uncharacterized sequence region with relatives found in fungal RT-like proteins. This part of Prp8 is predicted to adopt an alpha-helical structure and may be functionally equivalent to diverse maturase/X domains of retroelements and to the thumb domain of retroviral RTs. Together with a previously identified C-terminal domain that has an RNaseH-like fold, our results suggest evolutionary connections between Prp8 and ancient mobile elements. Prp8 may have evolved by acquiring nucleic acid-binding domains from inactivated retroelements, and their present-day role may be in maintaining proper conformation of the bound RNA cofactors and substrates of the splicing reaction. This is only the second example-the other one being telomerase-of the RT recruitment from a genomic parasite to serve an essential cellular function.
- Tuzel E
- Organelle dynamics: a tale of fusing nucleoli.
- Curr Biol. 2011; 21: 3957-3957
- Display abstract
Recent experiments on nucleoli suggest that their dynamic behavior is liquid-like with common fusion events and that the surrounding actin plays an active role in these dynamics.
- Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ
- The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing.
- Display abstract
The essential RNA helicase, Mtr4, performs a critical role in RNA processing and degradation as an activator of the nuclear exosome. The molecular basis for this vital function is not understood and detailed analysis is significantly limited by the lack of structural data. In this study, we present the crystal structure of Mtr4. The structure reveals a new arch-like domain that is specific to Mtr4 and Ski2 (the cytosolic homologue of Mtr4). In vivo and in vitro analyses demonstrate that the Mtr4 arch domain is required for proper 5.8S rRNA processing, and suggest that the arch functions independently of canonical helicase activity. In addition, extensive conservation along the face of the putative RNA exit site highlights a potential interface with the exosome. These studies provide a molecular framework for understanding fundamental aspects of helicase function in exosome activation, and more broadly define the molecular architecture of Ski2-like helicases.
- Chamousset D, Mamane S, Boisvert FM, Trinkle-Mulcahy L
- Efficient extraction of nucleolar proteins for interactome analyses.
- Proteomics. 2010; 10: 3045-50
- Display abstract
The efficient extraction of proteins from purified cellular organelles is critical for in vitro analyses, including identification of protein complex members by affinity purification-based quantitative proteomic approaches. When applied to purified nucleoli, classic nuclear protein extraction methods inefficiently and selectively release only approximately 50% of proteins. Here, we present a method that can extract up to 90% of nucleolar proteins, and apply it in a quantitative interactomic approach to identify nucleolar interaction partners for a mammalian protein phosphatase.
- Park AK, Kim H, Jin HJ
- Comprehensive phylogenetic analysis of evolutionarily conserved rRNA adenine dimethyltransferase suggests diverse bacterial contributions to the nucleus-encoded plastid proteome.
- Mol Phylogenet Evol. 2009; 50: 282-9
- Display abstract
The KsgA/Dim1 protein family of rRNA adenine dimethyltransferase (rAD) is well conserved throughout evolution. This protein family has been recognized to play multiple additional roles: as a mitochondrial transcription factor (mtTFB); as a yeast pre-rRNA cleavage enzyme (Dim1p); and as a chloroplast developmental protein (PFC1). Comprehensive phylogenetic analysis of rAD led to three main findings. First, rAD sequences were grouped by three domains of life, bacteria, archaea, and eukaryotes. Second, mtTFB shows alpha-proteobacterial endosymbiotic ancestry. Third, plastid-targeted rADs do not show cyanobacterial affiliation. Instead, plastid-targeted homologs from chlorophytes/land plants were clustered with chlamydiae, while those from rhodophytes/red algal lineage grouped with the bacteroides/chlorobi group. These unusual two-bacterial ancestries of plastid-targeted rAD suggest that bacterial genes influenced the evolution of the proteome of eukaryotic plastids in a complex way, involving more diverse bacterial groups than previously believed, and underscoring the importance of eukaryotic acquisition of bacterial functions.
- Shin HS, Jang CY, Kim HD, Kim TS, Kim S, Kim J
- Arginine methylation of ribosomal protein S3 affects ribosome assembly.
- Biochem Biophys Res Commun. 2009; 385: 273-8
- Display abstract
The human ribosomal protein S3 (rpS3), a component of the 40S small subunit in the ribosome, is a known multi-functional protein with roles in DNA repair and apoptosis. We recently found that the arginine residue(s) of rpS3 are methylated by protein arginine methyltransferase 1 (PRMT1). In this paper, we confirmed the arginine methylation of rpS3 protein both in vitro and in vivo. The sites of arginine methylation are located at amino acids 64, 65 and 67. However, mutant rpS3 (3RA), which cannot be methylated at these sites, cannot be transported into the nucleolus and subsequently incorporated into the ribosome. Our results clearly show that arginine methylation of rpS3 plays a critical role in its import into the nucleolus, as well as in small subunit assembly of the ribosome.
- McGuire AT, Keates RA, Cook S, Mangroo D
- Structural modeling identified the tRNA-binding domain of Utp8p, an essential nucleolar component of the nuclear tRNA export machinery of Saccharomyces cerevisiae.
- Biochem Cell Biol. 2009; 87: 431-43
- Display abstract
Utp8p is an essential 80 kDa intranuclear tRNA chaperone that transports tRNAs from the nucleolus to the nuclear tRNA export receptors in Saccharomyces cerevisiae. To help understand the mechanism of Utp8p function, predictive tools were used to derive a partial model of the tertiary structure of Utp8p. Secondary structure prediction, supported by circular dichroism measurements, indicated that Utp8p is divided into 2 domains: the N-terminal beta sheet and the C-terminal alpha helical domain. Tertiary structure prediction was more challenging, because the amino acid sequence of Utp8p is not directly homologous to any known protein structure. The tertiary structures predicted by threading and fold recognition had generally modest scores, but for the C-terminal domain, threading and fold recognition consistently pointed to an alpha-alpha superhelix. Because of the sequence diversity of this fold type, no single structural template was an ideal fit to the Utp8p sequence. Instead, a composite template was constructed from 3 different alpha-alpha superhelix structures that gave the best matches to different portions of the C-terminal domain sequence. In the resulting model, the most conserved sequences grouped in a tight cluster of positive charges on a protein that is otherwise predominantly negative, suggesting that the positive-charge cleft may be the tRNA-binding site. Mutations of conserved positive residues in the proposed binding site resulted in a reduction in the affinity of Utp8p for tRNA both in vivo and in vitro. Models were also derived for the 10 fungal homologues of Utp8p, and the localization of the positive charges on the conserved surface was found in all cases. Taken together, these data suggest that the positive-charge cleft of the C-terminal domain of Utp8p is involved in tRNA-binding.
- Wang F et al.
- A systematic survey of mini-proteins in bacteria and archaea.
- PLoS One. 2008; 3: 4027-4027
- Display abstract
BACKGROUND: Mini-proteins, defined as polypeptides containing no more than 100 amino acids, are ubiquitous in prokaryotes and eukaryotes. They play significant roles in various biological processes, and their regulatory functions gradually attract the attentions of scientists. However, the functions of the majority of mini-proteins are still largely unknown due to the constraints of experimental methods and bioinformatic analysis. METHODOLOGY/PRINCIPAL FINDINGS: In this article, we extracted a total of 180,879 mini-proteins from the annotations of 532 sequenced genomes, including 491 strains of Bacteria and 41 strains of Archaea. The average proportion of mini-proteins among all genomic proteins is approximately 10.99%, but different strains exhibit remarkable fluctuations. These mini-proteins display two notable characteristics. First, the majority are species-specific proteins with an average proportion of 58.79% among six representative phyla. Second, an even larger proportion (70.03% among all strains) is hypothetical proteins. However, a fraction of highly conserved hypothetical proteins potentially play crucial roles in organisms. Among mini-proteins with known functions, it seems that regulatory and metabolic proteins are more abundant than essential structural proteins. Furthermore, domains in mini-proteins seem to have greater distributions in Bacteria than Eukarya. Analysis of the evolutionary progression of these domains reveals that they have diverged to new patterns from a single ancestor. CONCLUSIONS/SIGNIFICANCE: Mini-proteins are ubiquitous in bacterial and archaeal species and play significant roles in various functions. The number of mini-proteins in each genome displays remarkable fluctuation, likely resulting from the differential selective pressures that reflect the respective life-styles of the organisms. The answers to many questions surrounding mini-proteins remain elusive and need to be resolved experimentally.
- Muro E, Hoang TQ, Jobart-Malfait A, Hernandez-Verdun D
- In nucleoli, the steady state of nucleolar proteins is leptomycin B-sensitive.
- Biol Cell. 2008; 100: 303-13
- Display abstract
BACKGROUND INFORMATION: The nucleolus is a dynamic structure. It has been demonstrated that nucleolar proteins rapidly associate with and dissociate from nucleolar components in continuous exchanges with the nucleoplasm using GFP (green fluorescent protein)-tagged proteins. However, how the exchanges within one nucleolus and between nucleoli within the nuclear volume occurred is still poorly understood. RESULTS: The movement of PAGFP (photoactivatable GFP)-tagged proteins that become visible after photoactivation can be followed. In the present study, we establish the protocol allowing quantification of the traffic of PAGFP-tagged nucleolar proteins in nuclei containing two nucleoli. The traffic in the activated area, at the periphery of the activated area and to the neighbouring nucleolus is measured. Protein B23 is rapidly replaced in the activated area, and at the periphery of the activated area the steady state suggests intranucleolar recycling of B23; this recycling is LMB (leptomycin B)-sensitive. The pool of activated B23 is equally distributed in the volume of the two nucleoli within 2 min. The three-dimensional distribution of the proteins Nop52 and fibrillarin is less rapid than that of B23 but is also LMB-sensitive. In contrast, traffic of fibrillarin from the nucleoli to the CB (Cajal body) was not modified by LMB. CONCLUSIONS: We propose that the steady state of nucleolar proteins in nucleoli depends on the affinity of the proteins for their partners and on intranucleolar recycling. This steady state can be impaired by LMB but not the uptake in the neighbouring nucleolus or the CB.
- Vesteg M, Krajcovic J
- Origin of eukaryotic cells as a symbiosis of parasitic alpha-proteobacteria in the periplasm of two-membrane-bounded sexual pre-karyotes.
- Commun Integr Biol. 2008; 1: 104-13
- Display abstract
The last universal common ancestor (LUCA) might have been either prokaryotic- or eukaryotic-like. Nevertheless, the universally distributed components suggest rather LUCA consistent with the pre-cell theory of Kandler. The hypotheses for the origin of eukaryotes are briefly summarized. The models under which prokaryotes or their chimeras were direct ancestors of eukaryotes are criticized. It is proposed that the pre-karyote (a host entity for alpha-proteobacteria) was a remnant of pre-cellular world, and was unlucky to have evolved fusion prohibiting cell surface, and thus could have evolved sex. The DNA damage checkpoint pathway could have represented the only pre-karyotic checkpoint control allowing division only when DNA was completely replicated without mistakes. The fusion of two partially diploid (in S-phase blocked) pre-karyotes might have represented another repair strategy. After completing replication of both haploid sets, DNA damage checkpoint would allow two subsequent rounds of fission. Alternatively, pre-karyote might have possessed two membranes inherited from LUCA. Under this hypothesis symbiotic alpha-proteobacterial ancestors of mitochondria might have ancestrally been selfish parasites of pre-karyote intermembrane space whose infection might have been analogous to infection of G(-)-bacterial periplasm by Bdellovibrio sp. It is suggested that eukaryotic plasma membrane might be derived from pre-karyote outer membrane and nuclear/ER membrane might be derived from pre-karyote inner membrane. Thus the nucleoplasm might be derived from pre-karyote cytoplasm and eukaryotic cytoplasm might be homologous to pre-karyote periplasm.
- Rohrmoser M et al.
- Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit.
- Mol Cell Biol. 2007; 27: 3682-94
- Display abstract
The PeBoW complex is essential for cell proliferation and maturation of the large ribosomal subunit in mammalian cells. Here we examined the role of PeBoW-specific proteins Pes1, Bop1, and WDR12 in complex assembly and stability, nucleolar transport, and pre-ribosome association. Recombinant expression of the three subunits is sufficient for complex formation. The stability of all three subunits strongly increases upon incorporation into the complex. Only overexpression of Bop1 inhibits cell proliferation and rRNA processing, and its negative effects could be rescued by coexpression of WDR12, but not Pes1. Elevated levels of Bop1 induce Bop1/WDR12 and Bop1/Pes1 subcomplexes. Knockdown of Bop1 abolishes the copurification of Pes1 with WDR12, demonstrating Bop1 as the integral component of the complex. Overexpressed Bop1 substitutes for endogenous Bop1 in PeBoW complex assembly, leading to the instability of endogenous Bop1. Finally, indirect immunofluorescence, cell fractionation, and sucrose gradient centrifugation experiments indicate that transport of Bop1 from the cytoplasm to the nucleolus is Pes1 dependent, while Pes1 can migrate to the nucleolus and bind to preribosomal particles independently of Bop1. We conclude that the assembly and integrity of the PeBoW complex are highly sensitive to changes in Bop1 protein levels.
- Buchhaupt M, Kotter P, Entian KD
- Mutations in the nucleolar proteins Tma23 and Nop6 suppress the malfunction of the Nep1 protein.
- FEMS Yeast Res. 2007; 7: 771-81
- Display abstract
The nucleolar Saccharomyces cerevisiae protein Nep1 was previously shown to bind to a specific site of the 18S rRNA and to be involved in assembly of Rps19p into pre-40S ribosome subunits. Here we report on the identification of tma23 and nop6 mutations as recessive suppressors of a nep1(ts) mutant allele and the nep1 deletion as well. Green fluorescent protein fusions localized Tma23p and Nop6p within the nucleolus, indicating their function in ribosome biogenesis. The high lysine content of both proteins and an RNA binding motif in the Nop6p amino acid sequence suggest RNA-binding functions for both factors. Surprisingly, in contrast to Nep1p, Tma23p and Nop6p seem to be specific for fungi as no homologues could be found in higher eukaryotes. In contrast to most other ribosome biogenesis factors, Tma23p and Nop6p are nonessential in S. cerevisiae. Interestingly, the tma23 mutants showed a considerably increased resistance against the aminoglycoside G418, probably due to a structural change in the 40S ribosomal subunit, which could be the result of incorrectly folded 18S rRNA gene, missing rRNA modifications or the lack of a ribosomal protein.
- Hinsby AM et al.
- A wiring of the human nucleolus.
- Mol Cell. 2006; 22: 285-95
- Display abstract
Recent proteomic efforts have created an extensive inventory of the human nucleolar proteome. However, approximately 30% of the identified proteins lack functional annotation. We present an approach of assigning function to uncharacterized nucleolar proteins by data integration coupled to a machine-learning method. By assembling protein complexes, we present a first draft of the human ribosome biogenesis pathway encompassing 74 proteins and hereby assign function to 49 previously uncharacterized proteins. Moreover, the functional diversity of the nucleolus is underlined by the identification of a number of protein complexes with functions beyond ribosome biogenesis. Finally, we were able to obtain experimental evidence of nucleolar localization of 11 proteins, which were predicted by our platform to be associates of nucleolar complexes. We believe other biological organelles or systems could be "wired" in a similar fashion, integrating different types of data with high-throughput proteomics, followed by a detailed biological analysis and experimental validation.
- Pal LR, Guda C
- Tracing the origin of functional and conserved domains in the human proteome: implications for protein evolution at the modular level.
- BMC Evol Biol. 2006; 6: 91-91
- Display abstract
BACKGROUND: The functional repertoire of the human proteome is an incremental collection of functions accomplished by protein domains evolved along the Homo sapiens lineage. Therefore, knowledge on the origin of these functionalities provides a better understanding of the domain and protein evolution in human. The lack of proper comprehension about such origin has impelled us to study the evolutionary origin of human proteome in a unique way as detailed in this study. RESULTS: This study reports a unique approach for understanding the evolution of human proteome by tracing the origin of its constituting domains hierarchically, along the Homo sapiens lineage. The uniqueness of this method lies in subtractive searching of functional and conserved domains in the human proteome resulting in higher efficiency of detecting their origins. From these analyses the nature of protein evolution and trends in domain evolution can be observed in the context of the entire human proteome data. The method adopted here also helps delineate the degree of divergence of functional families occurred during the course of evolution. CONCLUSION: This approach to trace the evolutionary origin of functional domains in the human proteome facilitates better understanding of their functional versatility as well as provides insights into the functionality of hypothetical proteins present in the human proteome. This work elucidates the origin of functional and conserved domains in human proteins, their distribution along the Homo sapiens lineage, occurrence frequency of different domain combinations and proteome-wide patterns of their distribution, providing insights into the evolutionary solution to the increased complexity of the human proteome.
- Hernandez-Verdun D
- The nucleolus: a model for the organization of nuclear functions.
- Histochem Cell Biol. 2006; 126: 135-48
- Display abstract
Nucleoli are the prominent contrasted structures of the cell nucleus. In the nucleolus, ribosomal RNAs (rRNAs) are synthesized, processed and assembled with ribosomal proteins. The size and organization of the nucleolus are directly related to ribosome production. The organization of the nucleolus reveals the functional compartmentation of the nucleolar machineries that depends on nucleolar activity. When this activity is blocked, disrupted or impossible, the nucleolar proteins have the capacity to interact independently of the processing activity. In addition, nucleoli are dynamic structures in which nucleolar proteins rapidly associate and dissociate with nucleolar components in continuous exchanges with the nucleoplasm. At the time of nucleolar assembly, the processing machineries are recruited in a regulated manner in time and space, controlled by different kinases and form intermediate structures, the prenucleolar bodies. The participation of stable pre-rRNAs in nucleolar assembly was demonstrated after mitosis and during development but this is an intriguing observation since the role of these pre-rRNAs is presently unknown. A brief report on the nucleolus and diseases is proposed as well as of nucleolar functions different from ribosome biogenesis.
- Hernandez-Verdun D
- Nucleolus: from structure to dynamics.
- Histochem Cell Biol. 2006; 125: 127-37
- Display abstract
The nucleolus, a large nuclear domain, is the ribosome factory of the cells. Ribosomal RNAs are synthesized, processed and assembled with ribosomal proteins in the nucleolus, and the ribosome subunits are then transported to the cytoplasm. In this review, the structural organization of the nucleolus and the dynamics of the nucleolar proteins are discussed in an attempt to link both information. By electron microscopy, three main nucleolar components corresponding to different steps of ribosome biogenesis are identified and the nucleolar organization reflects its activity. Time-lapse videomicroscopy and fluorescent recovery after photobleaching (FRAP) demonstrate that mobility of GFP-tagged nucleolar proteins is slower in the nucleolus than in the nucleoplasm. Fluorescent recovery rates change with inhibition of transcription, decreased temperature and depletion of ATP, indicating that recovery is correlated with cell activity. At the exit of mitosis, the nucleolar processing machinery is first concentrated in prenucleolar bodies (PNBs). The dynamics of the PNBs suggests a steady state favoring residence of processing factors that are then released in a control- and time-dependent manner. Time-lapse analysis of fluorescence resonance energy transfer demonstrates that processing complexes are formed in PNBs. Finally, the nucleolus appears at the center of several trafficking pathways in the nucleus.
- Thiry M, Lafontaine DL
- Birth of a nucleolus: the evolution of nucleolar compartments.
- Trends Cell Biol. 2005; 15: 194-9
- Display abstract
In eukaryotes, ribosome synthesis largely takes place in a specialized nuclear domain - the nucleolus. It has recently become apparent that this organelle is involved in the biogenesis of most cellular ribonucleoprotein particles (RNPs), as well as in cell-cycle regulation, making it central to gene expression. The field has traditionally acknowledged that each nucleolus is organized in three morphologically distinct compartments. Here, however, we discuss our view that in fact many eukaryotes have bipartite nucleoli. We propose that, during evolution, a third nucleolar compartment emerged at the transition between the anamniotes and the amniotes, following a substantial increase in size of the rDNA intergenic region. We believe that these conclusions have important implications for understanding the structure-function relationships within this key cellular organelle.
- Andersen JS et al.
- Nucleolar proteome dynamics.
- Nature. 2005; 433: 77-83
- Display abstract
The nucleolus is a key organelle that coordinates the synthesis and assembly of ribosomal subunits and forms in the nucleus around the repeated ribosomal gene clusters. Because the production of ribosomes is a major metabolic activity, the function of the nucleolus is tightly linked to cell growth and proliferation, and recent data suggest that the nucleolus also plays an important role in cell-cycle regulation, senescence and stress responses. Here, using mass-spectrometry-based organellar proteomics and stable isotope labelling, we perform a quantitative analysis of the proteome of human nucleoli. In vivo fluorescent imaging techniques are directly compared to endogenous protein changes measured by proteomics. We characterize the flux of 489 endogenous nucleolar proteins in response to three different metabolic inhibitors that each affect nucleolar morphology. Proteins that are stably associated, such as RNA polymerase I subunits and small nuclear ribonucleoprotein particle complexes, exit from or accumulate in the nucleolus with similar kinetics, whereas protein components of the large and small ribosomal subunits leave the nucleolus with markedly different kinetics. The data establish a quantitative proteomic approach for the temporal characterization of protein flux through cellular organelles and demonstrate that the nucleolar proteome changes significantly over time in response to changes in cellular growth conditions.
- Bjorklund AK, Ekman D, Light S, Frey-Skott J, Elofsson A
- Domain rearrangements in protein evolution.
- J Mol Biol. 2005; 353: 911-23
- Display abstract
Most eukaryotic proteins are multi-domain proteins that are created from fusions of genes, deletions and internal repetitions. An investigation of such evolutionary events requires a method to find the domain architecture from which each protein originates. Therefore, we defined a novel measure, domain distance, which is calculated as the number of domains that differ between two domain architectures. Using this measure the evolutionary events that distinguish a protein from its closest ancestor have been studied and it was found that indels are more common than internal repetition and that the exchange of a domain is rare. Indels and repetitions are common at both the N and C-terminals while they are rare between domains. The evolution of the majority of multi-domain proteins can be explained by the stepwise insertions of single domains, with the exception of repeats that sometimes are duplicated several domains in tandem. We show that domain distances agree with sequence similarity and semantic similarity based on gene ontology annotations. In addition, we demonstrate the use of the domain distance measure to build evolutionary trees. Finally, the evolution of multi-domain proteins is exemplified by a closer study of the evolution of two protein families, non-receptor tyrosine kinases and RhoGEFs.
- Gurchenkov VV, Polzikov MA, Magoulas C, Romanova LG, Zatsepina OV
- [Properties and functions of a new nucleolar protein, Surf-6, in 3T3 mouse cells].
- Bioorg Khim. 2005; 31: 578-85
- Display abstract
The localization of the specific protein Surf-6 from nucleoli of eukaryotic cells in mitosis and its sensitivity to the treatment of cells with RNase A and DNase I in situ were studied. It was shown that, in interphase nucleoli of 3T3 mouse cells, Surf-6 is probably associated with RNA and practically is not associated with DNA. In mitosis, Surf-6 appears in forming nucleoli after the known RNA-binding proteins fibrillarin and B23/nucleofozmin, which are involved in the early and late stages of the assembly of ribosomal particles, respectively. These observations and the regularities of migration of early and late proteins of ribosome assembly to nucleoli in the telophase of mitosis led us to the presumption that Surf-6 is involved in the terminal stages of the assembly of ribosomal particles in murine cells. An immunoblot analysis of the Surf-6 content in synchronized 3T3 cells showed for the first time that Surf-6 is present at all stages of the cell cycle but its content markedly decreases when cells enter the G0 period. Conversely, the activation of cells for proliferation is accompanied by an increase in the Surf-6 content. These observations allow one to regard Surf-6 as a marker of the cell proliferative state and suggest its implication in the regulation of the cell cycle. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2005, vol. 31, no. 6; see also http://www.maik.ru.
- Polzikov M, Zatsepina O, Magoulas C
- Identification of an evolutionary conserved SURF-6 domain in a family of nucleolar proteins extending from human to yeast.
- Biochem Biophys Res Commun. 2005; 327: 143-9
- Display abstract
The mammalian SURF-6 protein is localized in the nucleolus, yet its function remains elusive in the recently characterized nucleolar proteome. We discovered by searching the Protein families database that a unique evolutionary conserved SURF-6 domain is present in the carboxy-terminal of a novel family of eukaryotic proteins extending from human to yeast. By using the enhanced green fluorescent protein as a fusion protein marker in mammalian cells, we show that proteins from distantly related taxonomic groups containing the SURF-6 domain are localized in the nucleolus. Deletion sequence analysis shows that multiple regions of the SURF-6 protein are capable of nucleolar targeting independently of the evolutionary conserved domain. We identified that the Saccharomyces cerevisiae member of the SURF-6 family, named rrp14 or ykl082c, has been categorized in yeast databases to interact with proteins involved in ribosomal biogenesis and cell polarity. These results classify SURF-6 as a new family of nucleolar proteins in the eukaryotic kingdom and point out that SURF-6 has a distinct domain within the known nucleolar proteome that may mediate complex protein-protein interactions for analogous processes between yeast and mammalian cells.
- Deeds EJ, Shakhnovich B, Shakhnovich EI
- Proteomic traces of speciation.
- J Mol Biol. 2004; 336: 695-706
- Display abstract
Recent work has shown that the network of structural similarity between protein domains exhibits a power-law distribution of edges per node. The scale-free nature of this graph, termed the protein domain universe graph or PDUG, may be reproduced via a divergent model of structural evolution. The performance of this model, however, does not preclude the existence of a successful convergent model. To further resolve the issue of protein structural evolution, we explore the predictions of both convergent and divergent models directly. We show that when nodes from the PDUG are partitioned into subgraphs on the basis of their occurrence in the proteomes of particular organisms, these subgraphs exhibit a scale-free nature as well. We explore a simple convergent model of structural evolution and find that the implications of this model are inconsistent with features of these organismal subgraphs. Importantly, we find that biased convergent models are inconsistent with our data. We find that when speciation mechanisms are added to a simple divergent model, subgraphs similar to the organismal subgraphs are produced, demonstrating that dynamic models can easily explain the distributions of structural similarity that exist within proteomes. We show that speciation events must be included in a divergent model of structural evolution to account for the non-random overlap of structural proteomes. These findings have implications for the long-standing debate over convergent and divergent models of protein structural evolution, and for the study of the evolution of organisms as a whole.
- Leipe DD, Koonin EV, Aravind L
- STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer.
- J Mol Biol. 2004; 343: 1-28
- Display abstract
Using sequence profile analysis and sequence-based structure predictions, we define a previously unrecognized, widespread class of P-loop NTPases. The signal transduction ATPases with numerous domains (STAND) class includes the AP-ATPases (animal apoptosis regulators CED4/Apaf-1, plant disease resistance proteins, and bacterial AfsR-like transcription regulators) and NACHT NTPases (e.g. NAIP, TLP1, Het-E-1) that have been studied extensively in the context of apoptosis, pathogen response in animals and plants, and transcriptional regulation in bacteria. We show that, in addition to these well-characterized protein families, the STAND class includes several other groups of (predicted) NTPase domains from diverse signaling and transcription regulatory proteins from bacteria and eukaryotes, and three Archaea-specific families. We identified the STAND domain in several biologically well-characterized proteins that have not been suspected to have NTPase activity, including soluble adenylyl cyclases, nephrocystin 3 (implicated in polycystic kidney disease), and Rolling pebble (a regulator of muscle development); these findings are expected to facilitate elucidation of the functions of these proteins. The STAND class belongs to the additional strand, catalytic E division of P-loop NTPases together with the AAA+ ATPases, RecA/helicase-related ATPases, ABC-ATPases, and VirD4/PilT-like ATPases. The STAND proteins are distinguished from other P-loop NTPases by the presence of unique sequence motifs associated with the N-terminal helix and the core strand-4, as well as a C-terminal helical bundle that is fused to the NTPase domain. This helical module contains a signature GxP motif in the loop between the two distal helices. With the exception of the archaeal families, almost all STAND NTPases are multidomain proteins containing three or more domains. In addition to the NTPase domain, these proteins typically contain DNA-binding or protein-binding domains, superstructure-forming repeats, such as WD40 and TPR, and enzymatic domains involved in signal transduction, including adenylate cyclases and kinases. By analogy to the AAA+ ATPases, it can be predicted that STAND NTPases use the C-terminal helical bundle as a "lever" to transmit the conformational changes brought about by NTP hydrolysis to effector domains. STAND NTPases represent a novel paradigm in signal transduction, whereby adaptor, regulatory switch, scaffolding, and, in some cases, signal-generating moieties are combined into a single polypeptide. The STAND class consists of 14 distinct families, and the evolutionary history of most of these families is riddled with dramatic instances of lineage-specific expansion and apparent horizontal gene transfer. The STAND NTPases are most abundant in developmentally and organizationally complex prokaryotes and eukaryotes. Transfer of genes for STAND NTPases from bacteria to eukaryotes on several occasions might have played a significant role in the evolution of eukaryotic signaling systems.
- Scherl A et al.
- Functional proteomic analysis of human nucleolus.
- Mol Biol Cell. 2002; 13: 4100-9
- Display abstract
The notion of a "plurifunctional" nucleolus is now well established. However, molecular mechanisms underlying the biological processes occurring within this nuclear domain remain only partially understood. As a first step in elucidating these mechanisms we have carried out a proteomic analysis to draw up a list of proteins present within nucleoli of HeLa cells. This analysis allowed the identification of 213 different nucleolar proteins. This catalog complements that of the 271 proteins obtained recently by others, giving a total of approximately 350 different nucleolar proteins. Functional classification of these proteins allowed outlining several biological processes taking place within nucleoli. Bioinformatic analyses permitted the assignment of hypothetical functions for 43 proteins for which no functional information is available. Notably, a role in ribosome biogenesis was proposed for 31 proteins. More generally, this functional classification reinforces the plurifunctional nature of nucleoli and provides convincing evidence that nucleoli may play a central role in the control of gene expression. Finally, this analysis supports the recent demonstration of a coupling of transcription and translation in higher eukaryotes.
- Ospina JK, Matera AG
- Proteomics: the nucleolus weighs in.
- Curr Biol. 2002; 12: 2931-2931
- Display abstract
Numerous studies have indicated that the nucleolus is involved in a variety of cellular processes besides its well-known function in ribosome biosynthesis. A recent study describing the nucleolar proteome opens the way to new avenues of research on this important nuclear suborganelle.
- Couzin J
- Cell biology. Stripping the nucleolus down to its proteins.
- Science. 2002; 295: 422-422
- Swain T
- Protein evolution.
- Science. 1978; 201: 703-4
- Gayer J, Puza V
- A model of nucleolar structure and behaviour.
- Experientia. 1969; 25: 732-732
- Perry RP
- Nucleolus: structure and function.
- Science. 1966; 153: 214-9
- [Observations on the biochemical role of the nucleolus].
- Biochim Biophys Acta. 1954; 15: 263-7
- Lindegren CC
- The Origin of Volutin on the Chromosomes, Its Transfer to the Nucleolus, and Suggestions Concerning the Significance of this Phenomenon.
- Proc Natl Acad Sci U S A. 1948; 34: 187-93


text:
Concierge / Contact
Concierge Service 215.922.7392
E-Mail email@example.com
New York
725 Madison Ave.
New York, NY 10021
Mon - Sat 11-5
text 917.227.9039
1118 Walnut Street
Philadelphia, PA 19107
Mon – Thurs 10-5 - Fri 10-4
Shipping Rates
Paul Morelli offers complimentary standard overnight shipping, including insurance, for all online orders within the continental United States. International customers, as well as customers located outside of the continental United States, are responsible for shipping and insurance charges, including any taxes or customs duties. Paul Morelli generally uses FedEx for shipments, however, we may use any shipping service we deem appropriate. Please contact us with any special delivery requests.
Sales Tax & Prices
All prices on the website are shown in United States Dollars. Local taxes, including sales tax, if applicable, will be added to your order.
Care & Repair
If you would like to clean your jewelry at home, the only thing we suggest, without knowing the item needing cleaning, is scrubbing with an unused soft toothbrush & warm water. We would be happy to clean your jewelry if you would like to arrange to have it shipped to and from our studio in Philadelphia. Please contact the concierge with more questions.
Please contact our concierge regarding repairs. We treat them all differently depending on what needs to be repaired.
Returns & Exchanges
Due to the individual craftsmanship involved in every piece produced in our atelier, Paul Morelli does not accept returns and no refunds will be provided. You may exchange merchandise in accordance with the exchange policy set forth below. Exchanges of merchandise which are not in compliance with the conditions and timeframes set forth below may be rejected by Paul Morelli and will be sent back to you.
Exchange period
You may exchange merchandise purchased on the Website. The package containing the merchandise to be exchanged must be deposited with the shipper within seven (7) days of receipt of the merchandise.
Exchange process
If you wish to exchange merchandise, you must comply with the following steps:
Call 215.922.7392 or email email@example.com to request an exchange authorization. Paul Morelli will send a return shipping label to you. The shipping label is only valid on the date specified on the shipping label. Include the merchandise and all items and documents included with the merchandise in its original box. All shipments must be double boxed using new, unused FedEx shipping boxes. For example, the merchandise must be put in its original box, inside a FedEx medium box, inside a FedEx large box. Seal the delivery package and affix the return shipping label. Drop off the package at any staffed FedEx location (no drop boxes) or call FedEx to arrange for pick-up. If you call to arrange for pick-up, the package must be scanned into the FedEx system before the driver leaves the place of pick-up. You must obtain and keep your receipt. You must keep proof of return shipment. Paul Morelli accepts no liability in the event you are unable to produce such proof. Only merchandise received by Paul Morelli will be eligible for exchange. Upon receiving the merchandise, Paul Morelli will verify that the merchandise satisfies the conditions of the exchange policy.
Conditions to exchange merchandise
Paul Morelli products must be returned in a new and unused state, in perfect condition, with all protective materials in place and tags and stickers attached to them. Paul Morelli will not accept for exchange any merchandise that shows signs of wear, or has been used or altered from its original condition in any way.
Paul Morelli will not accept exchanges on any special orders, sized, altered, or engraved pieces.
All exchanges will be subject to strict review to ensure that the merchandise satisfies Paul Morelli's standards. If the merchandise does not meet these standards, Paul Morelli will refuse the exchange and the merchandise will be sent back to the customer. If the merchandise satisfies these standards, Paul Morelli will proceed with the exchange.
Merchandise credit
Upon verification that the merchandise satisfies the standards set forth above, Paul Morelli will issue a merchandise credit to the customer. Initial and return shipping charges, including insurance, will be the responsibility of the customer and will be deducted from the original amount paid by the customer before a credit is issued. Merchandise credit is valid for thirty (30) days and can be used toward the purchase price of items purchased on the Website or in the Paul Morelli studio.
Terms & Conditions
(The "Website") is a site operated by Paul Morelli Design, Inc., hereafter referred to as "Paul Morelli" or "we". Use of the Website is subject to the following Terms of Use (the "Terms"). Paul Morelli may revise these Terms from time to time by updating this page, with the revised Terms taking effect for all users as of the date stated on the posting. Your continued use of this Website following the posting of any changes indicates your acceptance of the changes. You should consult the Terms regularly.
Please read the Terms carefully before using the Website. You expressly acknowledge that you are aware of these Terms and have had access to the same upon entering the Website. Your use of the Website constitutes your agreement to the Terms. If you do not agree with the Terms, please do not use the Website.
All text, graphics, logos, button icons, images, audio clips, digital downloads, and data compilations, both individually and as they are compiled on the Website, and all software found on the Website are the property of Paul Morelli or our suppliers and are protected by United States and international copyright laws.
The trademarks or trade dress of Paul Morelli and our affiliates may not be used without our written permission. Trademarks or trade dress include the Paul Morelli name and other graphics, logos, page headers, button icons, scripts, and services name of Paul Morelli's products, services, and programs, and those of our affiliates.
Disclaimer of liability
Neither Paul Morelli nor its affiliates make any representation or warranty of any kind, express or implied, including without limitation that the Website will be uninterrupted or error-free, that defects will be corrected, or that the Website, including the server that makes it available, is free of viruses or other harmful components. Except as otherwise provided by applicable laws, in no event shall Paul Morelli, its affiliates, and each of their respective directors, officers, employees, agents, contractors, successors, and assigns, be liable for any direct, indirect, special, incidental, punitive, consequential or other damages arising out of or related to the use, inability to use, authorized use, performance or nonperformance of the Website, as well as to damages for lost profits, business interruption or the loss of data or information, even if Paul Morelli was previously advised of the possibility of such damages and regardless of whether such damages arise in contract, tort, under statute, in equity, at law or otherwise.
Governing law
Any claims, controversies, or disputes shall be governed by the laws of the Commonwealth of Pennsylvania, without regard to the principles of conflicts of law. Your use of the Website indicates your agreement that the laws of the Commonwealth of Pennsylvania, without regard to the principles of conflicts of laws, will govern any dispute of any sort that may arise between you and Paul Morelli and any of our affiliates. The disposition of any such dispute shall take place in a state or federal court located in Philadelphia, Pennsylvania. You consent to the exclusive jurisdiction and venue of such court.
You agree to indemnify Paul Morelli, its affiliates, and each of their respective directors, officers, employees, agents, contractors, successors, and assigns from and against all losses, expenses, damages and costs, including reasonable attorneys' fees, resulting from your violation of these Terms.
Entire agreement
These Terms (as amended from time to time) constitute the entire agreement between you and Paul Morelli regarding your use of the Website and any transactions you may have with Paul Morelli and its affiliates through the Website, and supersedes any other agreement or understanding, whether written or oral, between you and Paul Morelli with regard to the subject matter of the Terms.
Privacy Policy
Paul Morelli recognizes the importance of protecting the privacy of information collected about you.
The information we collect
Generally, you may browse the Website without providing any personally identifiable information. When placing an order, you may register and create an online account. During this process, you will be required to provide valid and current personal information, including but not limited to your name, phone number, billing information, and email address, as well as other personal information such as shipping address, billing address, and payment details (collectively, the "Personal Information").
From your purchases and other interactions with us, we obtain information concerning the specific products or services you purchase or use. When you visit this Website, our web server automatically collects anonymous information such as log data and IP addresses. We may use the automatically collected information for a number of purposes, such as improving our Website design, product assortments, customer service, and special promotions.
How we use the information we collect
We use this information to provide you with better service, in particular, for the following reasons:
to complete your purchase transactions, to provide the services you request, to keep you informed about the status of your orders, to send you our catalogs and other offerings by mail, to identify your product and service preferences, so we can notify you of new or additional products, services, and promotions that might be of interest, and internal record keeping.
The following information will be used jointly by Paul Morelli, PayPal, who provides the online payment portal, and your credit card company to process payment of your order: your name and address, your credit card information, the identification of the creations you have ordered, and the price paid for the creations you have ordered.
Others with whom we may share your information:
affiliates of Paul Morelli, third-party service providers and vendors we engage to help us run our business, carefully selected outside companies when we believe their products or services may be of interest to you, a purchaser or potential purchaser of our business. We may provide access to information when legally required to do so, to cooperate with police investigations or other legal proceedings, to protect against misuse or unauthorized use of this Website, to limit our legal liability and protect our rights or to protect the rights, property or safety of visitors of this Website or the public.
Your choices regarding use of the information we collect:
If you prefer to be removed from the list of customers that receive direct mail or telemarketing calls, please email: firstname.lastname@example.com, call: 215.922.7392 or write to: 1118 Walnut Street, Philadelphia, PA 19107, including your name and address and stating whether you wish to be removed from mail offers, phone offers, or both.
Children's Online Privacy Protection Act
This Website is directed to adults; it is not directed to children under the age of 13. We operate the Website in compliance with the Children's Online Privacy Protection Act, and will not knowingly collect or use personal information from anyone under 13 years of age.
In order to prevent unauthorized access or disclosure, we have put in place commercially reasonable physical, electronic, and administrative procedures to safeguard and secure the information we collect from you. In the absence of negligence on our part, we shall not be held liable for any loss you may suffer if a third party obtains unauthorized access to any Personal Information you provide to us.
Cookies are files that store information on your hard drive or browser that allow the Website to recognize that you have previously visited. We use cookies for certain areas of the Website, including but not limited to session cookies, persistent cookies and web beacons. We use cookies for things like keeping track of what is in your shopping cart, recording your session information, and improving the Website design and our customer service. You can disable cookies and web beacons on your computer by indicating this in the preferences or options menus in your browser.
Links to other sites
The Website may link to other websites which are not within our control. We do not make any representations or warranties about any website you may access through the Website. They are independent from us, and we have no control over, or responsibility for, their information or archives. Once you leave the Website, we cannot be responsible for the protection and/or privacy of any information you provide. Make sure you understand any website's privacy policies before providing personal information.
You will receive promotional emails only if you have asked to receive them. If you do not wish to receive emails, you can unsubscribe by sending an email to email@example.com.

subset: commoncrawl


text:
TRANSSEXUAL VANEZA PHOTOS 100% real South American Beauty A godsend. Ready to satisfy you and introduce you to the world of transsexuality, I am eager to experience multiple sexual relationships with you. Let's gather the stars in the sky and take pleasure in touching my soft skin. And from only 23 years old, the ultimate enjoyment that life has to do! * SERVICE MENU: I am active, passive and with remarkable detail, 100% functional, 69, mutually oral until the end, poppers, kisses with tongue, anal tongue with you (expert), all positions, erotic massages, latex costumes, fetish, (dildos), domination, parties ... and much more ... Guaranteed orgasm are you nervous because it's your first experience? ... relax!! Follow a perfect woman with an extra :-) I do everything slowly, no stress, no time pressure ... always with love: D There is always a first time for everything !!! I can't wait to see you! kisses Shemale VANEZA
Hello my love... I'm Ana, a very pretty and affectionate young woman, I'm always wet because I can't stop thinking about sex. I like to touch myself every day and I need a man like you. Kisses
HELLO TO ALL! I AM Carla BEAUTIFUL AS ON THE PHOTOS. IF YOU FEEL LIKE DISSING A GOOD MOMENT OF RELAXATION WITH A GOOD MASSAGE I THINK YOU HAVE FOUND THE RIGHT PERSON! I AM A VERY BEAUTIFUL AND VERY CLASSICAL Escort. I APPRECIATE KINDNESS, CLEANLINESS AND GOOD TIMES SPENT TOGETHER. MY PICTURES ARE REAL! FOR MORE INFORMATION DON'T HESITATE TO CALL ME, FOR AN APPOINTMENT JUST LET ME KNOW AN HOUR BEFORE. CALLS ARE BETTER THAN MAILS OR SMS. THANK YOU IN ADVANCE AND SEE YOU SOON KISSES...
HELLO TO ALL I RECEIVE IN PITTSBURG BEAUTIFUL TRANS BRUNETTE MY AD IS REAL, CALL ME AND YOU'LL SEE THAT I'M NOT A SCAM LIKE ALL THE OTHERS I am 1:78 cm 65 kg 32 years old sexy attractive and sweet I receive in an apparently renovated joule well decorated with good taste, discreet air conditioning and super clean two minutes from downtown easy to park, I don't answer messages and call privately, sorry. Big kisses to all Thank you and see you soon THANIA
I am Boris, to serve you :) I offer you sensual and deep massages. I will bring you relaxation and release, as well as voluptuousness until the forgetfulness of oneself... You will be able to discover different formulas of massages, which will allow you to choose the intensity of what you receive, and which I can give you... I offer my services to women, as well as to men, and to couples. I receive in an apartment, but can eventually move. Sensual and tantric massage, touch and voluptuousness. Erotic massage, with happy end (manual), or body-body are possibilities. For couples, a more participative form is possible (four-hand massage with one of the partners). Sensual massage: this is more of a discovery offer. Reconnecting with Tantric massage techniques, combining gentle massage and touch, this massage awakens your senses and takes you away in a pleasant voluptuousness. (The genitals are not touched, the person being massaged is naked, the masseur remains clothed). 1h, with oils. Erotic massage: The massage is deeper, it loosens your muscles, transports your body to an avalanche of sensations, the massage ends with a happy-end, only manual. (the person being massaged is naked, the masseur remains clothed). 1h, with oils. Body-body massage: The masseur will be naked, like the massee. The massage techniques will be similar to the previous massages, the masseur will use his whole body to massage the back and buttocks of the person being massaged. All the body is massaged, of course, and a happy-end is proposed, always only manual. (the masseur and the person being massaged are naked). ). 1h, with oils. The happy-end is an option, it can be replaced by a soft end of massage. These massages do not include sexual intercourse. Massages can take place at your home or at your hotel. I also receive downtown, communication of the address after reservation. Thank you for your understanding.
I move to Pittsburg, Le Touquet, wimereux, on the opal coast.....soirée, full night possible ...
HELLO I am diso on the champs elysees send message for any info 24 hours a day
I'm a sweet woman I'm ANASTASIA, I'm 42 years old I'm of Colombian-Spanish origin. I am a beautiful woman. To Make You Spend A Moment In My Company, I Receive At Home In Conviviality And In All Discretion Of course. I like to spend time with respectful and courteous men if you are looking for a moment with me. CALL ME YOU WILL NOT BE DISAPPOINTED
Hello, I am LARISSA a beautiful trans, I practice massages I live in a discreet apartment, I am ideal for your first time, come discover a new experience and spend a pleasant moment in my company all my photos are 100% real. Very perfect for beginners I'm dominatrix I am a full class trans with a touch of natural elegance, a beautiful body, skin like honey with an intense look and a mischievous smile. I have a lot of imagination, always in a good mood and not in a hurry. At the same time very sexy, I have a beautiful lingerie, I receive very sexy for massage. If I don't answer the calls, it's because I'm busy, leave a message so I can answer you. I offer you my complete services of massage, relaxation and relaxation . contact me . Thank you and see you soon
Hello, I'm Gisele, a beautiful trans passing through Pittsburg for a few days. My pictures are real, no bad surprise on the spot. I am active and passive, 19 cm very hard and thick. I take my time. I receive in a very discreet apartment (FREE PARKING BELOW THE BUILDING). Available from 9 am until midnight, appointment 30 min before. I don't answer to hidden calls and *s. Kisses and see you soon
Hi, I'm Stephanie a beautiful transsexual of 45 years old I have experience and knowledge ;) I'm tall, thin brunette, I have a big chest and a pulpy mouth waiting for you my loulous ! For the meetings I receive only in my apartment, condom mandatory my services are 30min and for more information on my conditions come to contact me if interested. Kisses ♡
Hello, my name is Joyce, a beautiful black woman with a sensual and tonic physique. I receive only in my private apartment to offer you a memorable moment! Don't hesitate to call for more info! See you soon!
I ahí beautiful Latina realle the city Enghien Les Bains, I am a beautiful woman, very sexy, extremely feminine and refined ... I have beautiful curves. Soft and intelligent. I love to share intense moments, unforgettable moments. So, if you appreciate discretion and confidentiality, if you are looking for a beautiful, sweet and intelligent company. I invite you to a meeting that should be unforgettable. I reserve myself for men of good taste. Call me 20 minutes before the appointment notes :) You can contact me by phone or SMS. If I do not answer at present, I am busy. Never answer when I'm with someone else. But don't worry, when I finish, I will give you an SMS. I do not answer hidden calls, emails and landline numbers.
Hello sensual brunette proposes to meet in respect and courtesy I can be very dominating Kiss
a black woman international sucker in the city with a soft skin in shape. likes to cuddle in a clean apartment does not answer sms
francaise few taboos and very talented I receive at home for a pleasant moment in the respect of each one.....I only answer the calls it assures you that I am not a fake ....a very fast kisses.....
Sex: Woman Ethnicity: Latin Nationality: Brazilian Age: 30 Eyes: Brown Height: 170 cm high Weight: 70 Kg Hair: Light chestnut Bust-size hip: 90-60-90 Cup: C Bikini waxing: Fully shaved Alcohol: Occasionally Smoke: Yes Languages: American: Portuguese: Spanish: Hours of work: Monday: 08:00 - 23:00 hrs. Tuesday: 08:00 am - 11:00 pm Wednesday: 08:00 am - 11:00 pm Thursday: 08:00 - 11:00 pm Friday: 08:00 - 11:00 PM Saturday: 08:00 - 11:00 PM Sunday: 08:00 - 11:00 pm About Me Hello, I suis⭐FEMME Charlotte 30 YEARS ⭐ of BRAZILIAN origin and I am here to give you pleasure. I am a family with a good experience and education, I am also friendly. If you want to have a good time, I am the one for you. ✅Je is complete, I offer kissing, caresses, massage, 69 and blowjob. ✔ Friendliness, impeccable hygiene and discretion are de rigueur for both parties so that you have a very good time relaxing in my company. I am above all with the listening of your desires. I privilege a meeting, a true exchange, and not a botched service. I will know how to put you at ease, because I prefer quality meetings to quantity. The photos on line are recent and it's me : I am NOT AN ARNAQUE. for you to be pleasant thank you to call me 30 min before coming to see me. a very fast kiss.
Hi my name is Mia, young refined and sexy student. I receive in private apartment on the city of Pittsburg. I meet only man of forty years and more impeccable hygiene and respect required ⚠ First contacts by SMS with your age origin please
Françoise 42 years old slut shemale, passive bareback. Submissive with beautiful ass very cambered on the Pittsburg area Research for taking in hand and making available in various places, active guys loving sex and wanting to test beautiful shemale.
I am a young girl trav and very naughty, I like passive men who like to be dominated, I am also passive with a good ass and sweet to enjoy, a dowry always hard and with milk for you.
Beautiful TRANS... I am active and passive and I can be active and dominant or hot passive ... I am up to what you want. I have 19cm very hard and fully functional to make you have a good time with passion and pleasure with lots of warm milk. Whatever you want, I hope it will come true. If you want to be with me! My goal is to pamper you, to be the kind of service that the most demanding gentlemen come back for again and again. Always give you the best experience. My fees are 100% non-negotiable, as you would expect from any professional. ... SATISFACTION ALWAYS GUARANTEED .... I am ready to make your fantasies come true ... Very open-minded for new things, all kinds of FANTASIES and FETISHES!
Hello my loves! I am a sophisticated and ardent woman who will make you spend incredible moments, simply you will be able to meet me, I like respectful gentlemen and maximum hygiene. You can find me in my apartment located in Pittsburg, a relaxed and sensual atmosphere that you will surely appreciate, I answer calls and sms, I hope to see you soon!
Hello my name is Jade Dominatrix I'm 19 years old, Brazilian I'm very active 22 cm with a lot of semen! Also with erotic massage, blowjob, kisses and ejaculation I'm like the picture. I am a calm and patient professional with beginners, I demand respect.
Hi my love , My name is Melina, I am young, and I am here to show you a very good time. Lonely men who need presence to relax? Call me to spend a pleasant moment in my company.


text:
Iae is the Moon god for the Mamaiurans, an Amazon tribe that lives in Brazil. According to a Mamaiuran legend, at the beginning of time there were so many birds in the sky that their wings prevented daylight from being seen. It was always night and the people lived in fear of attack from wild animals.Tired of the darkness, two heroes, Iae and his brother Kuat, decided to
force the king of the birds, Urubutsin, to share some of the daylight with the people of the Amazon.
The two brothers hid inside a dead animal and waited for the birds to
approach. As soon as Urubutsin landed, Kuat grabbed his leg. Unable to
get away, Urubutsin was forced to make an agreement with the two brothers.
The birds would share daylight with the Mamaiurans, and day would
alternate with night. Since then, Kuat represented the Sun and Iae the Moon.


text:
Iwill XA100 Aladdin V Super7 Board
by Anand Lal Shimpi on May 25, 1998 1:58 PM EST- Posted in
- Motherboards
As Intel demolishes the Socket-7 environment with their Celeron/EX on the low end and their Deschutes/BX combos on the high end, a manufacturer needs to stay swift in order to outrun the competition in this industry. Simply cranking out TX motherboards or even Socket-7 AGP boards doesn't cut it anymore, users demand more and they are not willing to pay the outrageous prices for a Slot-1 motherboard, what else is a manufacturer to do but meet these demands on the low end with a high end Socket-7 motherboard.
The above factoid can be found on the box and User's Manual of Iwill's newest AGP Socket-7 motherboard, the XA100. What sets the XA100 apart from the competition is the chipset the board was built around, Acer Lab's (ALi) Aladdin V, a Super7 (Socket-7 + AGP + 100MHz Front Side Bus) chipset.
Anand Tech Report Card Rating
CPU Interface | Socket-7 |
Chipset | ALi Aladdin V |
L2 Cache | 512KB |
Form Factor | ATX |
Bus Speeds | 60 / 66 / 75 / 83 / 100 MHz |
Clock Multipliers | 2.0x - 5.5x |
Voltages Supported | 1.8v / 2.1v / 2.2v / 2.7v / 2.8v / 2.9v / 3.2v / 3.5v |
Memory Slots | 3 168pin DIMM Slots (EDO/SDRAM) |
Expansion Slots | 1 AGP Slot 4 PCI Slots 3 ISA Slots (1 Shared / 3 Full Length) |
Why follow the rest of the pack when you can set your own trends? This seemed to be Iwill's intention with the XA100, at a first glance the eye catching box the board arrived in depicted a pack of 3 Cheetahs (the animals, not the hard drives ;)...) against an African sunset backdrop, a highly unusual image for a motherboard, however if Iwill's intention was to be different they definitely accomplished it. Lifting up the top of the motherboard box doesn't reveal a cluttered assortment of cables and documentation, instead you see a cardboard pop-up bearing the logo: "Iwill -- Make Things Happen." | |
This cover contains information on how to obtain technical support, the Iwill homepage address (listed about 4 times total), as well as some other interesting information about the company itself. Removing this cover thankfully doesn't reveal another one, instead you find the manual on top of the XA100, underneath which lies a box containing the proper HDD/FDD cables necessary to get your system up and running. Looking at the board itself produces a unique sight, the arctic gray color that is found on the PCI slots, IDE/FDC connectors, and the CPU socket is a very rare occurrence, although it does add a pleasing appearance to the motherboard. The ATX form factor Super7 board features a healthy 4 PCI, 3 ISA, and 1 AGP expansion slot layout complimenting the 3 DIMM slots for memory expansion. Courtesy of the Aladdin V chipset the XA100 can cache above 64MB of RAM, more specifically, a full 128MB cacheable memory area is possible with only 512KB of L2 cache. One of the unique qualities the Aladdin V chipset boasts is the internal L2 cache the chipset features, more specifically the M1541 chip has an integrated 16K x 10-bit Tag RAM as well as 16K x 2 L2 cache SRAM, both of which decrease cost and increase performance at the same time. For this reason you can expect an Aladdin V board to be cheaper than an equivalently equipped VIA MVP3 Super7 board. |
The board itself looks like some of the newer BX motherboards in terms of size and layout, the XA100 closely resembles the ASUS P2B with the exception of the presence of a Socket-7 CPU interface. The upper left hand corner of the motherboard is home to an extremely tiny and out of the way green power LED indicator, a feature that can be found on most Tyan motherboards. Closer to the Socket-7 IC (Integrated Circuit) you'll find a sparse population of small to mid-sized Vendell capacitors, including some between the ATX Power Supply Connector and the CPU Socket in order to decrease fluctuations in the voltage supplied to your CPU and therefore increase stability. The voltage regulators on the XA100 don't feature heatsinks on them, however this failed to pose a problem during the reliability tests AnandTech conducted. Closer to the AGP slot you'll find the 456-pin M1541 Aladdin V chipset which makes the 100MHz Front Side Bus possible on the XA100. |
Tapping the power of the Aladdin V chipset is done through the use of an Epox-like single jumper configuration setup. A single jumper controls the clock multiplier settings while another controls the Front Side Bus speed selection, allowing you to choose from a list ranging from 60 - 100MHz, all of which operated in an extremely stable manner. Whatever problems plagued the Aladdin V chipset previously seemed to have been solved as Iwill proved to the world that they can construct a Super7 board built around this elusive chipset. The Aladdin V allows for Pseudo-Synchronous operation of the PCI/AGP Buses keeping them at around 33 and 66MHz respectively, removing the possibility of running into problems with your PCI/AGP peripherals. On the ISA end, the AMI BIOS allows you to manually set the AT Clock Frequency in order to prevent any problems your ISA peripherals may have.
The User's Manual provided by Iwill is a step away from the 'el-cheapo' User's Manual you're probably used to seeing packaged with ALi based motherboards, Iwill paid great attention to detail in the manual and although there is some room for improvement it is definitely a well made document. Also packaged with the motherboard are the ALi AGP GART VxD Drivers and the ALi Bus Master IDE drivers as well, both were installed for the AnandTech tests and each installation went without any problems at all.
Performance-wise, the XA100 blows away all standard Socket-7 motherboards as it allows for Pentium MMX and AMD K6 owners to take advantage of the 100MHz Front Side Bus Frequency, unfortunately the Cyrix 6x86MX tested didn't seem to want to work at the 100MHz FSB speed. Simply switching to the 100MHz FSB speed provides an average of a 10% increase in performance over its 66MHz counterpart, this is definitely a feature you'll need in order to get the full performance out of AMD's new K6-2 processor.
A 112MHz bus speed would have been nice, apparently FIC's VA-503+ (MVP3) does feature this setting and initial reports state that it is quite stable, however the 100MHz bus speed will have to do for now. Like the Epox Super7 Motherboard, the XA100 doesn't feature any CPU core voltage settings between 2.2v and 2.7v, making overclocking the K6-300 to 350 (100 x 3.5) virtually impossible. Other than those two oversights the XA100 is a job well done by Iwill.


text:
Story highlights
NEW: The NYPD says Boeing has confirmed the part came from a 767
NEW: Both planes that slammed into the twin towers were 767s
Police believe the piece is part of a landing gear from one of the 9/11 airliners
The medical examiner will do an examination for human remains, Kelly says
A piece believed to be from one of the airliners that hit the World Trade Center towers on September 11, 2001, has been found behind the site of an Islamic community center near ground zero, the New York Police Department said Friday.
Investigators are looking into how a part of what appears to be landing gear became wedged between 51 Park Place – the site of a controversial community center – and another building, just a few blocks from ground zero.
"If you see how confined this space is, and you realize the chaos that existed on this street, I think it's understandable. It's not that surprising," NYPD Commissioner Ray Kelly said.
"It's very, very confined and no construction work went on, or no clean up went on in this 18-inch space between the two buildings" after the attacks.
Even so, he said investigators are looking at all possibilities, including whether the part was intentionally placed between the two buildings.
"We are also looking into a possibility it was lowered by a rope," Kelly said, adding that a piece of rope appeared to be intertwined with the part.
But Kelly said an initial survey found no marks on the walls between the two buildings consistent with such an object being lowered. He also it appears that there is a break in the rope and that it came down from the roof on top of the plane part.
National Transportation Safety Board investigators will determine whether the part is from either United Airlines Flight 175 or American Airlines Flight 11, which hit the twin towers, he said.
Police have said the part includes "a clearly visible Boeing identification number." On Saturday, the NYPD said police investigators had been in touch with Boeing, which confirmed the part is from one of its 767 aircraft. Both flights that hit the World Trade Center towers were 767s.
American Airlines and United Airlines declined to comment.
Boeing spokesman John Dern confirmed the company was asked to "examine the images to see what can be determined."
The part was discovered Wednesday by surveyors hired by a property owner. They called 911 to report that they'd found "apparently damaged machinery," police said.
"The NYPD is securing the location as it would a crime scene, documenting it photographically," the police statement said.
The plane part will not be moved until after the medical examiner's office completes a health and safety inspection.
"The office of the chief medical examiner will do an in-depth examination of the site to see if there are, in fact, human remains there," Kelly said.
New York police officers were standing guard through the weekend outside the buildings. Investigators are expected to return Monday to determine how to remove the part.
The plane part is about five feet long, four feet wide and 17 inches deep, Kelly said.
The discovery of the plane part comes more than 11 years after the two airliners slammed into the towers of the World Trade Center.
"Well, obviously, this is a manifestation of a horrific terrorist attack a block and a half away from where we stand," Kelly said. "So sure, it brings back terrible memories to anyone who was here and anyone who was involved in that event."
Sally Regenhard, whose son Christian – a probationary firefighter – died when the towers collapsed, said she was not surprised by the find.
"I'm disgusted, because after 9/11 the proper search was never done. The whole aftermath was uncoordinated. It was inadequate," she said.
Regenhard has been one of the leading voices and, at times, critics for the families of the September 11 victims, pushing hard for a federal investigation and calling for a more comprehensive search for remains and debris.
"We advocated for a huge trajectory from that collapse," she said. "Human remains were thrown at least for a mile, but probably two or three miles from the site."
In the years since, a number of pieces of debris as well as human remains have been discovered in Lower Manhattan.
"We are cooperating fully with the appropriate authorities to make sure this piece of evidence is removed with care as quickly and effectively as possible," said Sharif El-Gamal, president of Soho Properties, the owner of 51 Park Place.
The building had been the site of furious protests, pitting those opposed to putting an Islamic center near ground zero and those who say it is a center meant to bring people together.
Rob Frehse reported from New York; Chelsea J. Carter reported and wrote from Atlanta. CNN's Lorenzo Ferrigno and Chris Kokenes contributed to this report.


text:
Reinstate the Indefinite Leave to Remain visas for the Boyd family
Gary Boyd is a British citizen, born and raised in Edinburgh, Scotland. He has been married to Kristee Boyd for 9 years and has been a devoted stepfather to Kyle for the same period of time. The Boyd family lived together in the UK for 2 years, from 2004 – 2006, and, in 2006, Kristee and Kyle were granted Indefinite Leave to Remain (ILR) visas, which specifically state that they are valid "indefinitely." After leaving the UK for 5 years to work in the field of international education, the Boyd family returned to the UK for Gary to take up a permanent Depute Head Teacher position at Kirkwall Grammar School in Orkney, Scotland. However, they were surprised to learn upon their return that Indefinite Leave to Remain visas are not, in fact, "indefinite" but expire after two years of living abroad. This is the case even though the Boyd family maintained strong ties to the UK and returned to holiday with family and friends on numerous occasions over the years spent living overseas. The UK Border Agency is currently advising the Boyds to follow their rules, which require Kristee and Kyle to travel to Australia to apply for the appropriate entry clearance to return to their home in Orkney. This could involve waiting in Australia for a period of up to 6 months. This would involve: (i) removing Kyle from his 4th year studies (final year of Standard Grade education) and (ii) removing both children (as Kristee is Nyah's primary caregiver)from their Dad, to live separately from him for up to 6 months. We, the undersigned, call on the UK Border Agency to exhibit a sense of decency and an appreciation of family values by reinstating Kristee and Kyle's ILR visas and approving an 'outwith the rules' application, thereby allowing the family to continue to live together.
Scottish Parliament
The following motion in support of our family was lodged in the Scottish Parliament on 27th June 2012 by Liam McArthur. MSP (Liberal Democrat) and supported by Jamie Hepburn, MSP (SNP), Rhoda Grant, MSP (Labour), Linda Fabiani, MSP (SNP).
Some articles published in the local, regional and national media and press about our case include:
'Government should not be shifting blame' George Galloway, Member of Parliament, in Daily Record, 11th June 2012.
'Border Agency to split family.' Scottish Sunday Express, 10th June 2012
'MSPs slam UKBA over Boyd family break up threat.' Scottish National Party Press Release, 10th June 2012
'Agency deportation threat sparks anger.' Morning Star, 10th June 2012
'Island deputy headteacher caught up in visa wrangle.' The Herald Scotland, 30th May 2012
'Kirkwall Grammar School teacher's family faces removal from UK.' The Orcadian, 24th May 2012


text:
Can someone please help me, I'm looking for a way to find the main parent product category of a WooCommerce product? Say, the product is marked under Gadgets, but the main parent of them all is Electronics.
I want this per post, as I want to add a class to each post signifying its main parent product_cat
Please remember, product categories are custom taxonomy, and cannot be retrieved using get_category_parents()
. They are listed as terms.
Thanks in advance.
// edit:
This is the code I have already, I'm calling this on each post and my posts are rendered similar to an archive page.
function all_cat_classes($post) {
$cats = "";
$terms = get_the_terms($post->ID, "product_cat");
$count = 0;
$count = count($terms);
$key = 0;
foreach ($terms as $cat) {
return $cats;


text:
Buddhism and Western Science
March 1, 2012 | papal
The Bodhisattva's Brain: Buddhism Naturalized by Owen Flanagan — Having authored several books and article on the philosophy of mind and cognitive science, Owen Flanagan's perspective on the intersection of Buddhism, psychology and Western philosophy is well informed and generally unbiased. Bracketing supernatural elements that are inconsistent with science, this treatise emphasizes the practical potential of Buddhist spirituality for attaining a philosophically informed state of happiness. Buddhist principles are examined in light of Aristotle's emphasis on reason and virtue, with added focus on compassion.


text:
Maritime Soap design by Izola
Izola is proud to offer these handcrafted authentic soaps in the style of fine 18th century toiletries. This old world triple milled recipe is an all-vegetable base with the moisturizing benefit of olive oil.This is an environmentally sensitive soap made with vegetable oils and is free of animal testing. Raw materials are domestically sourced. We print with soy based inks on post consumer recycled paper. Made with Organic Oatmeal.The ingredients in our milled soaps are: olive oil, cocoa butter, shea butter, essential oils and a vegetable soap base. Each soap weighs 6 oz.Made in the USA. Maritime Please allow 1-2 weeks to ship out and receive tracking.


text:
Published 12:00 am Tuesday, January 1, 2013
TAMPA, Fla. — Steve Spurrier's plan to use two quarterbacks in the Outback Bowl worked so well that Dylan Thompson and Connor Shaw both earned game balls.
That's a first for the Head Ball Coach, who has a well-known penchant for benching struggling QBs. Except in this case, the Gamecocks' winningest coach used his talented pair of passers by design.
Shaw began Tuesday's 33-28 victory over Michigan with a 56-yard touchdown pass to Damiere Byrd. Thompson closed it out by throwing a 32-yard TD strike to Bruce Ellington in the final minute to help South Carolina match the school record for victories in a season.
"I don't know if I've ever given two quarterbacks a game ball, but today I said: 'Hey, we've got to give them to both you guys,'" Spurrier said.
"Both those young men are just so super team-oriented. There's no jealousy, nothing. … Those guys are just really, really good teammates. Wonderful team players," the coach added. "We tried to tell Connor: 'It's your game.' And it was his game, but Dylan was going to play. He understood that. It worked beautifully as it turned out."
Thompson replaced Shaw during the winning drive, covering the final 43 yards after Shaw began the march from his own 30 and kept it alive with a 6-yard completion to Ace Sanders on a fourth-and-3 play. Devin Gardner's third TD pass of the game had given Michigan a 28-27 lead.
"I wasn't nervous. I knew I had great guys around me, and I trusted them and just was confident," Thompson said.
Shaw threw for 227 yards and two touchdowns after missing the Gamecocks' regular-season finale with a left foot sprain. Thompson led the Gamecocks (11-2) to a victory at archrival Clemson, and threw for 117 yards and two TDs in the bowl.
Gardner threw for 214 yards in his fifth start for Michigan (8-5) since Denard Robinson injured his right elbow late in the season. Robinson took some snaps at quarterback and even attempted his first passes in a game since Oct. 27, but lined up mostly at running back and rushed for 100 yards on 23 carries.
Sanders caught TD passes of 4 yards from Thompson and 31 yards from Shaw, who completed 18 of 26 passes before aggravating his foot injury and limping off during the final drive. The speedy receiver had nine catches for 92 yards and also scored on a 63-yard punt return — one of four plays over 50 yards yielded by Michigan.
Gardner was 18 of 36, including TD passes of 5 yards to Drew Dileo and 10 and 17 yards to Jeremy Gallon, who gave Michigan its late lead and finished with career bests of nine receptions and 145 yards. Robinson set the NCAA record for career yards rushing by a quarterback, hiking his four-year total to 4,495 — 15 more than West Virginia's Pat White ran for from 2005-08.
"I'd rather win the game," said Robinson, who attempted two passes in the third quarter, both incompletions, and also ran twice on plays in which he took the snap as the quarterback — a role he's embraced since being injured during a loss to Nebraska.
"It was just what I thought it was going to be," Robinson said. "I tried to make the most of it."
South Carolina defensive end Jadeveon Clowney was quiet for much of the day, but shifted momentum in the fourth quarter with a big hit on Vincent Smith that sent the running back's helmet rolling several yards backward and caused a fumble that the SEC defensive player of the year recovered to set up Shaw's TD pass to Sanders for a 27-22 lead.
The TD capped a three-play sequence that began with Michigan running its second fake punt of the game, gaining 4 yards to the Wolverines 41 for what was ruled a first down, despite not appearing be one when the officials called for a measurement. South Carolina challenged the spot, but the ruling on the field was upheld.
Clowney then slammed into Smith just as the Michigan runner was taking the handoff from Gardner, jarring the ball loose.
"I asked one of those other refs there. I said, 'You know the ball did not touch the first-down marker.' He said, 'I know it didn't.' I said, 'Well, why did he give it to them?' and he said, 'I don't know,'" Spurrier said.
"Clowney knocked the ball out the next play, so I'm glad they gave it to them. … We gained about 10 or 15 yards."
Robinson was injured during the first half of Michigan's two-touchdown loss to Nebraska on Oct. 27. He missed the rest of that game, as well the next two against Minnesota and Northwestern before returning the final two weeks of the regular season to contribute in ways that didn't require him to throw the ball.
The 6-foot, 197-pound native of Deerfield Beach, Fla., entered the game during Michigan's second possession and ran for 15 yards on his first play.
Gardner threw 26 yards to Gallon, moving the Wolverines into position for Brendan Gibbons to kick a 39-yard field goal.
Down 14-3 after Sanders' punt return, Michigan marched 75 yards in 11 plays to trim South Carolina's lead to four, with Robinson carrying four times for 20 yards along the way.
Michigan began the day ranked second in the nation in pass defense, allowing 155 yards per game. South Carolina matched that in the opening half alone.
on Shaw's long TD throw to Byrd and Thompson's 70-yard completion to Jones that led to Sanders' second TD for a 21-10 lead.
The Wolverines turned South Carolina's only turnover into Gibbons' 40-yard field goal in the second quarter, and Matt Wile's Outback Bowl-record 52-yard field goal trimmed Michigan's deficit to 21-16.
South Carolina ended on a five-game winning streak that followed consecutive losses to LSU and Florida. The Gamecocks also won 11 games last season.
"We hit eight of 10 goals we started the season with," Spurrier said. "We did that last year, too. That's good, but it still can be better."